Poly [ADP-ribose] polymerase (PARP1) is a DNA-repair enzyme that adds ADP-ribose groups to nuclear proteins. Mutating position 762 from valine to alanine (V762A) in PARP1 is correlated with lung cancer and follicular lymphoma. Molecular dynamics simulations were performed on three versions of PARP1: the wild type (WT), a mutated version containing V762A (V762A), and a mutated structure created by editing the wild type structure (V762A-from-WT), in order to determine the effect of the mutation on the protein's movements and energy interactions. Root mean square deviation (RMSD) analysis suggested that average RMSD for WT is higher than that of V762A, indicating a difference in dynamics. Matrix correlations, which reveal correlated movements, suggest that V762A-from-WT behaves like V762A, not WT. Additionally, energy decomposition analysis (EDA) was performed to identify attractive or repulsive interactions within the protein. Together, matrix correlation analysis, V762A-from-WT-V762A EDA difference plots, and WT-V762A EDA difference plots identified residues near 875 as a region of interest. Root mean square fluctuations (RMSF), WT-V762A-from-WT EDA difference plots, and WT-V762A EDA difference plots marked residues near the mutation (near residue 762) as a region of interest. Overall, these changes suggest that the V762A mutation impacts the dynamics of PARP1. Further study is needed to understand the connection between the mutation and the region containing residue 875.